|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
65-321 |
1.91e-59 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 191.36 E-value: 1.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 65 RIITLTNSDMGIVYALGG--SVVGRQTMDASGVEPSAALKATEVGNTHDLNLEKIASLTPDVIIASSEQNL-KDVPALEG 141
Cdd:COG0614 2 RIVSLSPSATELLLALGAgdRLVGVSDWGYCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDeEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 142 IGAQVVLTGANSIADIKKQEAILGQLLGKD--ATNLQKEIDQKVAEIKQE--QTGKAVRALLILGAPGSNYAALPNSLSG 217
Cdd:COG0614 82 IGIPVVVLDPRSLEDLYESIRLLGELLGREerAEALIAEYEARLAAVRARlaGAEERPTVLYEIWSGDPLYTAGGGSFIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 218 DILEAAGGVNVAKDFKGvenfpQYASLNIEKIVESDPEVIFLMiHGGDEKETELAFQKEMKQNDAWNSTTAVKNNHIVVL 297
Cdd:COG0614 162 ELLELAGGRNVAADLGG-----GYPEVSLEQVLALDPDVIILS-GGGYDAETAEEALEALLADPGWQSLPAVKNGRVYVV 235
|
250 260
....*....|....*....|....
gi 738133139 298 PADLFgTNPGIRITKALDYMANEL 321
Cdd:COG0614 236 PGDLL-SRPGPRLLLALEDLAKAL 258
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
67-300 |
2.06e-35 |
|
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 426291 [Multi-domain] Cd Length: 233 Bit Score: 128.25 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 67 ITLTNSDMGIVYALGG--SVVGRQTMDASGVEPSAALKATEVGNTHDLNLEKIASLTPDVIIASSEQNLKDVPALEGIGA 144
Cdd:pfam01497 1 AALSPAYTEILYALGAtdSIVGVDAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 145 QVVLTGANS-IADIKKQEAILGQLLGKD--ATNLQKEIDQKVAEIKQ---EQTGKAVrALLILGAPGSNYAALPNSLSGD 218
Cdd:pfam01497 81 PTVIFESSStGESLKEQIKQLGELLGLEdeAEELVAEIDSALAAAKKavpSLTRKPV-LVFGGADGGGYVVAGSNTYIGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 219 ILEAAGGVNVAKDFKGVEnfpqYASLNIEKIVESDPEVIFLMIHGGDEKEtelaFQKEMKQNDAWNSTTAVKNNHIVVLP 298
Cdd:pfam01497 160 LLRILGIENIAAELSGSE----YAPISFEAILSSNPDVIIVSGRDSFTKT----GPEFVAANPLWAGLPAVKNGRVYTLP 231
|
..
gi 738133139 299 AD 300
Cdd:pfam01497 232 SD 233
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
64-319 |
4.40e-33 |
|
Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238564 [Multi-domain] Cd Length: 245 Bit Score: 122.41 E-value: 4.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 64 ERIITLTNSDMGIVYALGGS--VVGRqtmDASGVEPSAALKATEVGNTHDLNLEKIASLTPDVIIASSEQNLK-DVPALE 140
Cdd:cd01144 1 MRIVSLAPSATELLYALGLGdqLVGV---TDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCaVVDQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 141 GIGAQVVLTGANSIADIKKQEAILGQLLGKD--ATNLQKEIDQKVAEIKQEQTGKA-VRALLILG-----APGSNYaalp 212
Cdd:cd01144 78 AAGIPVLVSEPQTLDDILADIRRLGTLAGRParAEELAEALRRRLAALRKQYASKPpPRVFYQEWidplmTAGGDW---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 213 nslSGDILEAAGGVNVAKDFKgvENFPQyasLNIEKIVESDPEVIFLMIHGGDEKETELafqkemKQNDAWNSTTAVKNN 292
Cdd:cd01144 154 ---VPELIALAGGVNVFADAG--ERSPQ---VSWEDVLAANPDVIVLSPCGFGFTPAIL------RKEPAWQALPAVRNG 219
|
250 260
....*....|....*....|....*..
gi 738133139 293 HIVVLPADLFGtNPGIRITKALDYMAN 319
Cdd:cd01144 220 RVYAVDGNWYF-RPSPRLVDGLEQLAA 245
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
47-321 |
2.14e-22 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 96.13 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 47 LTITDMAGRTINFAKKPERIITLTNSDMGIVYALGG--SVVG--RQTMDASGVEpsaalKATEVGNTHD--LNLEKIASL 120
Cdd:PRK09534 44 VTETDATGTEITLDERPERVVTLNPSAAQTMWELGArdRVVGvtQYASYLDGAE-----ERTNVSGGQPfgVNVEAVVGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 121 TPDVIIASSEQNLKDVPALEGIGAQVV-LTGANSIADIKKQEAILGQLLG--KDATNLQKEIDQKVAEIKQE--QTGKAV 195
Cdd:PRK09534 119 DPDLVLAPNAVAGDTVTRLREAGITVFhFPAATSIEDVAEKTATIGRLTGncEAAAETNAEMRDRVDAVEDRtaDVDDRP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 196 RALLILGapgSNYAALPNSLSGDILEAAGGVNVAKDfkgvENFPQYASLNIEKIVESDPEVIFLMIHGGDEKETElafqk 275
Cdd:PRK09534 199 RVLYPLG---DGYTAGGNTFIGALIEAAGGHNVAAD----ATTDGYPQLSEEVIVQQDPDVIVVATASALVAETE----- 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 738133139 276 emkqndAWNSTTAVKNNHIVVLPADLFgTNPGIRITKALDYMANEL 321
Cdd:PRK09534 267 ------PYASTTAGETGNVVTVNVNHI-NQPAPRIVESMATMATAF 305
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
65-321 |
1.91e-59 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 191.36 E-value: 1.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 65 RIITLTNSDMGIVYALGG--SVVGRQTMDASGVEPSAALKATEVGNTHDLNLEKIASLTPDVIIASSEQNL-KDVPALEG 141
Cdd:COG0614 2 RIVSLSPSATELLLALGAgdRLVGVSDWGYCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDeEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 142 IGAQVVLTGANSIADIKKQEAILGQLLGKD--ATNLQKEIDQKVAEIKQE--QTGKAVRALLILGAPGSNYAALPNSLSG 217
Cdd:COG0614 82 IGIPVVVLDPRSLEDLYESIRLLGELLGREerAEALIAEYEARLAAVRARlaGAEERPTVLYEIWSGDPLYTAGGGSFIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 218 DILEAAGGVNVAKDFKGvenfpQYASLNIEKIVESDPEVIFLMiHGGDEKETELAFQKEMKQNDAWNSTTAVKNNHIVVL 297
Cdd:COG0614 162 ELLELAGGRNVAADLGG-----GYPEVSLEQVLALDPDVIILS-GGGYDAETAEEALEALLADPGWQSLPAVKNGRVYVV 235
|
250 260
....*....|....*....|....
gi 738133139 298 PADLFgTNPGIRITKALDYMANEL 321
Cdd:COG0614 236 PGDLL-SRPGPRLLLALEDLAKAL 258
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
44-326 |
3.81e-37 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 134.16 E-value: 3.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 44 AAVLTITDMAGRTINFAKKPERIITLTNSDMGIVYALG--GSVVGRqtmDASGVEPSAALKATEVGNTHDLNLEKIASLT 121
Cdd:COG4558 8 LLLLALAALAAGASVAAAAAERIVSLGGSVTEIVYALGagDRLVGV---DTTSTYPAAAKALPDVGYMRQLSAEGILSLK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 122 PDVIIASSE-QNLKDVPALEGIGAQVV-LTGANSIADIKKQEAILGQLLGKD--ATNLQKEIDQKVAEIKQE--QTGKAV 195
Cdd:COG4558 85 PTLVLASEGaGPPEVLDQLRAAGVPVVvVPAAPSLEGVLAKIRAVAAALGVPeaGEALAARLEADLAALAARvaAIGKPP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 196 RALLILG-APGSNYAALPNSLSGDILEAAGGVNVAKDFKGvenfpqYASLNIEKIVESDPEVIFLMIHGGDEKETElafq 274
Cdd:COG4558 165 RVLFLLSrGGGRPMVAGRGTAADALIRLAGGVNAAAGFEG------YKPLSAEALIAAAPDVILVMTRGLESLGGV---- 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 738133139 275 KEMKQNDAWNSTTAVKNNHIVVLPADLFgTNPGIRITKALDYMANELNQVSK 326
Cdd:COG4558 235 DGLLALPGLAQTPAGKNKRIVAMDDLLL-LGFGPRTPQAALALAQALYPAAA 285
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
67-300 |
2.06e-35 |
|
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 426291 [Multi-domain] Cd Length: 233 Bit Score: 128.25 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 67 ITLTNSDMGIVYALGG--SVVGRQTMDASGVEPSAALKATEVGNTHDLNLEKIASLTPDVIIASSEQNLKDVPALEGIGA 144
Cdd:pfam01497 1 AALSPAYTEILYALGAtdSIVGVDAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 145 QVVLTGANS-IADIKKQEAILGQLLGKD--ATNLQKEIDQKVAEIKQ---EQTGKAVrALLILGAPGSNYAALPNSLSGD 218
Cdd:pfam01497 81 PTVIFESSStGESLKEQIKQLGELLGLEdeAEELVAEIDSALAAAKKavpSLTRKPV-LVFGGADGGGYVVAGSNTYIGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 219 ILEAAGGVNVAKDFKGVEnfpqYASLNIEKIVESDPEVIFLMIHGGDEKEtelaFQKEMKQNDAWNSTTAVKNNHIVVLP 298
Cdd:pfam01497 160 LLRILGIENIAAELSGSE----YAPISFEAILSSNPDVIIVSGRDSFTKT----GPEFVAANPLWAGLPAVKNGRVYTLP 231
|
..
gi 738133139 299 AD 300
Cdd:pfam01497 232 SD 233
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
64-319 |
4.40e-33 |
|
Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238564 [Multi-domain] Cd Length: 245 Bit Score: 122.41 E-value: 4.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 64 ERIITLTNSDMGIVYALGGS--VVGRqtmDASGVEPSAALKATEVGNTHDLNLEKIASLTPDVIIASSEQNLK-DVPALE 140
Cdd:cd01144 1 MRIVSLAPSATELLYALGLGdqLVGV---TDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCaVVDQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 141 GIGAQVVLTGANSIADIKKQEAILGQLLGKD--ATNLQKEIDQKVAEIKQEQTGKA-VRALLILG-----APGSNYaalp 212
Cdd:cd01144 78 AAGIPVLVSEPQTLDDILADIRRLGTLAGRParAEELAEALRRRLAALRKQYASKPpPRVFYQEWidplmTAGGDW---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 213 nslSGDILEAAGGVNVAKDFKgvENFPQyasLNIEKIVESDPEVIFLMIHGGDEKETELafqkemKQNDAWNSTTAVKNN 292
Cdd:cd01144 154 ---VPELIALAGGVNVFADAG--ERSPQ---VSWEDVLAANPDVIVLSPCGFGFTPAIL------RKEPAWQALPAVRNG 219
|
250 260
....*....|....*....|....*..
gi 738133139 293 HIVVLPADLFGtNPGIRITKALDYMAN 319
Cdd:cd01144 220 RVYAVDGNWYF-RPSPRLVDGLEQLAA 245
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
61-315 |
7.29e-32 |
|
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.
Pssm-ID: 238566 [Multi-domain] Cd Length: 256 Bit Score: 119.70 E-value: 7.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 61 KKPERIITLTNSDMGIVYALGGSVVG---RQTMDASGVEPSAALKATE-VGNTHDLNLEKIASLTPDVIIASSEQNLKDV 136
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVGvadTAGYKPWIPEPALPLEGVVdVGTRGQPNLEAIAALKPDLILGSASRHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 137 PALEGIGAQVVLTGANSIADIKKQEAILGQLLGK--DATNLQKEIDQKVAEIKQ---EQTGKAVrALLILGAPGSNYAAL 211
Cdd:cd01146 81 DQLSQIAPTVLLDSSPWLAEWKENLRLIAKALGKeeEAEKLLAEYDQRLAELRQklpDKGPKPV-SVVRFSDAGSIRLYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 212 PNSLSGDILEAAGGVNVAKDFKGVENFpqYASLNIEKIVESDPEVIFLMiHGGDEKetelaFQKEMKQNDAWNSTTAVKN 291
Cdd:cd01146 160 PNSFAGSVLEDLGLQNPWAQETTNDSG--FATISLERLAKADADVLFVF-TYEDEE-----LAQALQANPLWQNLPAVKN 231
|
250 260
....*....|....*....|....
gi 738133139 292 NHIVVLPADLFGTNPGIRITKALD 315
Cdd:cd01146 232 GRVYVVDDVWWFFGGGLSAARLLL 255
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
58-321 |
8.99e-30 |
|
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238560 [Multi-domain] Cd Length: 270 Bit Score: 114.28 E-value: 8.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 58 NFAKKPERIITLTNSDMGIVYALGGSVVGRqtmdASGVEPSAALKA------TEVGNTHDLNLEKIASLTPDVIIASSEQ 131
Cdd:cd01140 7 KVPKNPEKVVVFDVGALDTLDALGVKVVGV----PKSSTLPEYLKKykddkyANVGTLFEPDLEAIAALKPDLIIIGGRL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 132 NlKDVPALEGIGAQVVLT--GANSIADIKKQEAILGQLLGKD--ATNLQKEIDQKVAEIKQEQTGKAvRALLILGAPGSN 207
Cdd:cd01140 83 A-EKYDELKKIAPTIDLGadLKNYLESVKQNIETLGKIFGKEeeAKELVAEIDASIAEAKSAAKGKK-KALVVLVNGGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 208 YAALPNSLSGDILEAAGGVNVAKDfkgVENFPQYASLNIEKIVESDPEVIFLMIHG-GDEKETELAfqKEMKQNDAWNST 286
Cdd:cd01140 161 SAFGPGSRFGWLHDLLGFEPADEN---IKASSHGQPVSFEYILEANPDWLFVIDRGaAIGAEGSSA--KEVLDNDLVKNT 235
|
250 260 270
....*....|....*....|....*....|....*
gi 738133139 287 TAVKNNHIVVLPADLFGTNPGirITKALDYMANEL 321
Cdd:cd01140 236 TAWKNGKVIYLDPDLWYLSGG--GLESLKQMIDDL 268
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
61-259 |
3.08e-29 |
|
Periplasmic binding protein YvrC. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria and archaea. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238563 [Multi-domain] Cd Length: 195 Bit Score: 110.83 E-value: 3.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 61 KKPERIITLTNSDMGIVYALGGS--VVGRQTMDasgVEPSAALKATEVGNTHDLNLEKIASLTPDVIIASSEQNLKDVPA 138
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAGdkIVGVDTYS---NYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAELLEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 139 LEGIGAQVVLTG-ANSIADIKKQEAILGQLLGKD--ATNLQKEIDQKVAEIKQEQTGKAVRALLILGAPGSNYAALPNSL 215
Cdd:cd01143 78 LKDAGIPVVVLPaASSLDEIYDQIELIGKITGAEeeAEKLVKEMKQKIDKVKDKGKTIKKSKVYIEVSLGGPYTAGKNTF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 738133139 216 SGDILEAAGGVNVAKDFKGvenFPQyasLNIEKIVESDPEVIFL 259
Cdd:cd01143 158 INELIRLAGAKNIAADSGG---WPQ---VSPEEILKANPDVIIL 195
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-321 |
1.69e-28 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 111.94 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 1 MKKILIISLFSLLLVLMAACGpkeigssgnTSEKTSKQKVSEEAAVlTITDMAGrTINFAKKPERIITLTNSDMGIVYAL 80
Cdd:COG4594 1 MKKLLLLLILLLALLLLAACG---------SSSSDSSSSEAAAGAR-TVKHAMG-ETTIPGTPKRVVVLEWSFADALLAL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 81 GGSVVGrqTMDASGVEP-----SAALKATE-VGNTHDLNLEKIASLTPDVIIASSEQNLKDVPALEGIGAQVVL-TGANS 153
Cdd:COG4594 70 GVTPVG--IADDNDYDRwvpylRDLIKGVTsVGTRSQPNLEAIAALKPDLIIADKSRHEAIYDQLSKIAPTVLFkSRNGD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 154 IADIKKQEAILGQLLGKD--ATNLQKEIDQKVAEIKQ--EQTGKAVRALLILGAPGSNYAALPNSLSGDILEAAGGVNVA 229
Cdd:COG4594 148 YQENLESFKTIAKALGKEeeAEAVLADHDQRIAEAKAklAAADKGKKVAVGQFRADGLRLYTPNSFAGSVLAALGFENPP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 230 KDFKgVENFPqYASLNIEKIVESDPEVIFLMiHGGDEKetelaFQKEMKQNDAWNSTTAVKNNHIVVLPADLFGTNPGIr 309
Cdd:COG4594 228 KQSK-DNGYG-YSEVSLEQLPALDPDVLFIA-TYDDPS-----ILKEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGRGP- 298
|
330
....*....|..
gi 738133139 310 itKALDYMANEL 321
Cdd:COG4594 299 --LAAELMADDL 308
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-307 |
3.31e-28 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 111.04 E-value: 3.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 1 MKKILIISLFSLLLVLMAACGPKEigssgntsektSKQKVSEEAAVLTITDMAGrTINFAKKPERIITLtnsDMGIVyal 80
Cdd:COG4607 1 MKKTLLAALALAAALALAACGSSS-----------AAAASAAAAETVTVEHALG-TVEVPKNPKRVVVF---DNGAL--- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 81 ggsvvgrQTMDASGVEPSAALKAT--------------EVGNTHDLNLEKIASLTPDVIIASSEQNlKDVPALEGIGAQV 146
Cdd:COG4607 63 -------DTLDALGVEVAGVPKGLlpdylskyaddkyaNVGTLFEPDLEAIAALKPDLIIIGGRSA-KKYDELSKIAPTI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 147 VLT--GANSIADIKKQEAILGQLLGK--DATNLQKEIDQKVAEIKqEQTGKAVRALLILGAPG--SNYAalPNSLSGDIL 220
Cdd:COG4607 135 DLTvdGEDYLESLKRNTETLGEIFGKedEAEELVADLDAKIAALK-AAAAGKGTALIVLTNGGkiSAYG--PGSRFGPIH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 221 EAAGGVNVAKDFKgVENFPQYASLniEKIVESDPEVIFLMihggD-----EKETELAfqKEMKQNDAWNSTTAVKNNHIV 295
Cdd:COG4607 212 DVLGFKPADEDIE-ASTHGQAISF--EFIAEANPDWLFVI----DrdaaiGGEGPAA--KQVLDNELVKQTTAWKNGQIV 282
|
330
....*....|..
gi 738133139 296 VLPADLFGTNPG 307
Cdd:COG4607 283 YLDPDAWYLAGG 294
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
63-297 |
1.32e-27 |
|
Hemin binding protein HutB. These proteins have been shown to function as initial receptors in ABC transport of hemin and hemoproteins in many eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238569 [Multi-domain] Cd Length: 235 Bit Score: 107.74 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 63 PERIITLTNSDMGIVYALGG--SVVGRqtmDASGVEPSAALKATEVGNTHDLNLEKIASLTPDVIIASSEQNLKDV-PAL 139
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAgdRLVGV---DSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPEAlDQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 140 EGIGAQVV-LTGANSIADIKKQEAILGQLLGKD--ATNLQKEIDQKVAEIKQE--QTGKAVRALLILGAPGSN-YAALPN 213
Cdd:cd01149 78 RAAGVPVVtVPSTPTLDGLLTKIRQVAQALGVPekGEALAQEVRQRLAALRKTvaAHKKPPRVLFLLSHGGGAaMAAGRN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 214 SLSGDILEAAGGVNVAKDFKGvenfpqYASLNIEKIVESDPEVIFLMIHGGDEKETELAFqkemKQNDAWNSTTAVKNNH 293
Cdd:cd01149 158 TAADAIIALAGAVNAAAGFRG------YKPLSAEALIAAQPDVILVMSRGLDAVGGVDGL----LKLPGLAQTPAGRNKR 227
|
....
gi 738133139 294 IVVL 297
Cdd:cd01149 228 ILAM 231
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
54-318 |
1.77e-25 |
|
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238568 [Multi-domain] Cd Length: 284 Bit Score: 103.19 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 54 GRTINFAKKPERIITLTNSDMGIVYALG--GSVVGRQTMDaSGVEP--SAALKATEVGNTHDLNLEKIASLTPDVIIAS- 128
Cdd:cd01148 9 GRSVTFDKAPQRVVSNDQNTTEMMLALGlqDRMVGTAGID-NKDLPelKAKYDKVPELAKKYPSKETVLAARPDLVFGGw 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 129 ----SEQNLKDVPALEGIGAQVVL--------TGANSIADIKKQEAILGQLLGK--DATNLQKEIDQKVAEI--KQEQTG 192
Cdd:cd01148 88 sygfDKGGLGTPDSLAELGIKTYIlpescgqrRGEATLDDVYNDIRNLGKIFDVedRADKLVADLKARLAEIsaKVKGDG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 193 KAVRALLILGAPGSNYAALPNSLSGDILEAAGGVNVAKDFKGVenfpqYASLNIEKIVESDPEVIfLMIHGGDEKETELA 272
Cdd:cd01148 168 KKVAVFVYDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDES-----WTTVSWETVIARNPDVI-VIIDYGDQNAAEQK 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 738133139 273 fQKEMKQNDAWNSTTAVKNNHIVVLPADlfGTNPGIRITKALDYMA 318
Cdd:cd01148 242 -IKFLKENPALKNVPAVKNNRFIVLPLA--EATPGIRNVDAIEKLA 284
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
43-298 |
8.16e-25 |
|
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238562 [Multi-domain] Cd Length: 289 Bit Score: 101.28 E-value: 8.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 43 EAAVLTITDMAGRTINFAKKPERIITLTNSDMGIVYALGGS--VVGRQTM---DASGVEPSAALKATEVGNTH-DLNLEK 116
Cdd:cd01142 4 TAATRTITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGklIVATTSTvqqEPWLYRLAPSLENVATGGTGnDVNIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 117 IASLTPDVIIASSEQNlkdvpaLEGIGAQVVLTGANSIADIKKQE-----AILGQLLG--KDATNLQKEIDQKVAEIKqE 189
Cdd:cd01142 84 LLALKPDVVIVWSTDG------KEAGKAVLRLLNALSLRDAELEEvkltiALLGELLGrqEKAEALVAYFDDNLAYVA-A 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 190 QT-----GKAVRALLILGAPGSnyAALPNSLSGDILEAAGGVNVAKDfKGVENFPQYaslNIEKIVESDPEVIFLMihGG 264
Cdd:cd01142 157 RTkklpdSERPRVYYAGPDPLT--TDGTGSITNSWIDLAGGINVASE-ATKKGSGEV---SLEQLLKWNPDVIIVG--NA 228
|
250 260 270
....*....|....*....|....*....|....
gi 738133139 265 DEKetelafqKEMKQNDAWNSTTAVKNNHIVVLP 298
Cdd:cd01142 229 DTK-------AAILADPRWQNLRAVKNGRVYVNP 255
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
59-303 |
3.15e-24 |
|
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238567 [Multi-domain] Cd Length: 262 Bit Score: 99.33 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 59 FAKKPERIITLTNSDMGIVYALGG----SVVGRQTMDASG------VEPSAALKAT-EVGNTHDLNLEKIASLTPDVIIA 127
Cdd:cd01147 1 VPKPVERVVAAGPGALRLLYALAApdkiVGVDDAEKSDEGrpyflaSPELKDLPVIgRGGRGNTPNYEKIAALKPDVVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 128 ----SSEQNLKDVPALEGIgAQVVLTGANSIADIKKQEAILGQLLGKD---------ATNLQKEIDQKVAEIKQEQTGKA 194
Cdd:cd01147 81 vgsdDPTSIADDLQKKTGI-PVVVLDGGDSLEDTPEQIRLLGKVLGKEeraeelisfIESILADVEERTKDIPDEEKPTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 195 VRALLILGAPGSNYAALPNSlsGDILEAAGGVNVAKDFKGVENFpqyaSLNIEKIVESDPEVIFLmihggDEKETELAFQ 274
Cdd:cd01147 160 YFGRIGTKGAAGLESGLAGS--IEVFELAGGINVADGLGGGGLK----EVSPEQILLWNPDVIFL-----DTGSFYLSLE 228
|
250 260
....*....|....*....|....*....
gi 738133139 275 KEMKQNDAWNSTTAVKNNHIVVLPADLFG 303
Cdd:cd01147 229 GYAKNRPFWQSLKAVKNGRVYLLPALPFN 257
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
47-321 |
2.14e-22 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 96.13 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 47 LTITDMAGRTINFAKKPERIITLTNSDMGIVYALGG--SVVG--RQTMDASGVEpsaalKATEVGNTHD--LNLEKIASL 120
Cdd:PRK09534 44 VTETDATGTEITLDERPERVVTLNPSAAQTMWELGArdRVVGvtQYASYLDGAE-----ERTNVSGGQPfgVNVEAVVGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 121 TPDVIIASSEQNLKDVPALEGIGAQVV-LTGANSIADIKKQEAILGQLLG--KDATNLQKEIDQKVAEIKQE--QTGKAV 195
Cdd:PRK09534 119 DPDLVLAPNAVAGDTVTRLREAGITVFhFPAATSIEDVAEKTATIGRLTGncEAAAETNAEMRDRVDAVEDRtaDVDDRP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 196 RALLILGapgSNYAALPNSLSGDILEAAGGVNVAKDfkgvENFPQYASLNIEKIVESDPEVIFLMIHGGDEKETElafqk 275
Cdd:PRK09534 199 RVLYPLG---DGYTAGGNTFIGALIEAAGGHNVAAD----ATTDGYPQLSEEVIVQQDPDVIVVATASALVAETE----- 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 738133139 276 emkqndAWNSTTAVKNNHIVVLPADLFgTNPGIRITKALDYMANEL 321
Cdd:PRK09534 267 ------PYASTTAGETGNVVTVNVNHI-NQPAPRIVESMATMATAF 305
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
61-302 |
3.38e-21 |
|
Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238558 [Multi-domain] Cd Length: 248 Bit Score: 90.47 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 61 KKPERIITLTNSDMGIVyALGGSVVGrqTMDASGVEPSAA--LKATEVGNTHDLNLEKIASLTPDVIIASSEQNlKDVPA 138
Cdd:cd01138 7 AKPKRIVALSGETEGLA-LLGIKPVG--AASIGGKNPYYKkkTLAKVVGIVDEPNLEKVLELKPDLIIVSSKQE-ENYEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 139 LEGIGAQVVLTGANSiaDIKKQEAILGQLLGKD--ATNLQKEIDQKVAEIKQE--QTGKAVRALLILGAPGSNYA-ALPN 213
Cdd:cd01138 83 LSKIAPTVPVSYNSS--DWEEQLKEIGKLLNKEdeAEKWLADYKQKAKEAKEKikKKLGNDKSVAVLRGRKQIYVfGEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 214 SLSGDILEAAGGVNVAKDFKGVENFPQYASLNIEKIVESDPEVIFLMIHGGDEKETELafqkemKQNDAWNSTTAVKNNH 293
Cdd:cd01138 161 RGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFTGPEAKADF------ESLPIWKNLPAVKNNH 234
|
....*....
gi 738133139 294 IVVLPADLF 302
Cdd:cd01138 235 VYIVDAWVF 243
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
47-294 |
1.13e-20 |
|
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238559 [Multi-domain] Cd Length: 342 Bit Score: 90.83 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 47 LTITDMAGRTINFAKKPERIITLTNSDMGIVYALGGS-----VVGRQTmDASGVEPSAALKATE----------VGNTH- 110
Cdd:cd01139 1 ITVTDVAGRKVTLDAPVERVLLGEGRQLYALALLEGEnpfarIVGWGG-DLKKGDPDTYAKYKEkfpeiadiplIGSTYn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 111 -DLNLEKIASLTPDVII-----ASSEQNLKDVPALEGIGAQVVLTG------ANSIADIKkqeaILGQLLGKD--ATNLQ 176
Cdd:cd01139 80 gDFSVEKVLTLKPDLVIlniwaKTTAEESGILEKLEQAGIPVVFVDfrqkplKNTTPSMR----LLGKALGREerAEEFI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 177 KEIDQKVAEI-----KQEQTGKAVRALLILGAPGSNYAALPNSLSGDILEAAGGVNVAKDFKGVEnfpqYASLNIEKIVE 251
Cdd:cd01139 156 EFYQERIDRIrdrlaKINEPKPKVFIELGAGGPEECCSTYGNGNWGELVDAAGGDNIADGLIPGT----SGELNAEYVIA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 738133139 252 SDPEVIFL-------------MIHGGDEKETELAFQKEMKQNDAWNSTTAVKNNHI 294
Cdd:cd01139 232 ANPEIIIAtggnwakdpsgvsLGPDGTTADAKESLLRALLKRPGWSSLQAVKNGRV 287
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
64-188 |
6.49e-16 |
|
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.
Pssm-ID: 238347 [Multi-domain] Cd Length: 148 Bit Score: 73.75 E-value: 6.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 64 ERIITLTNSDMGIVYALGGS--VVGRQTMDASGVEPSAAL-KATEVGNTHDLNLEKIASLTPDVIIASSEQNLKDVPALE 140
Cdd:cd00636 1 KRVVALDPGATELLLALGGDdkPVGVADPSGYPPEAKALLeKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWLDKLS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 738133139 141 GIGAQVVLT---GANSIADIKKQEAILGQLLGK--DATNLQKEIDQKVAEIKQ 188
Cdd:cd00636 81 KIAIPVVVVdeaSELSLENIKESIRLIGKALGKeeNAEELIAELDARLAELRA 133
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
41-324 |
3.11e-10 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 60.07 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 41 SEEAAVLTITDMAGrTINFAKKPERIITLTNSDMGIVYALGGSVVG-RQTMDASGVEPS--AALKA-TEVGNTHDLNLEK 116
Cdd:PRK11411 18 SSHAFAVTVQDEQG-TFTLEKTPQRIVVLELSFVDALAAVGVSPVGvADDNDAKRILPEvrAHLKPwQSVGTRSQPSLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 117 IASLTPDVIIASSEQNLKDVPALEGIGAQVVLTGAN-SIADIKKQEAILGQLLGKDAtNLQKEID---QKVAEIKQeQTG 192
Cdd:PRK11411 97 IAALKPDLIIADSSRHAGVYIALQKIAPTLLLKSRNeTYQENLQSAAIIGEVLGKKR-EMQARIEqhkERMAQFAS-QLP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 193 KAVRALLILGAPGSNYAALPNSLSGDILEAAgGVNVAKdfKGVENFPqYASLNIEKIVESDPEVIFLmIHGGDEketelA 272
Cdd:PRK11411 175 KGTRVAFGTSREQQFNLHSPESYTGSVLAAL-GLNVPK--APMNGAA-MPSISLEQLLALNPDWLLV-AHYRQE-----S 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 738133139 273 FQKEMKQNDAWNSTTAVKNNHIVVLPADLFGTNPGIritKALDYMANELNQV 324
Cdd:PRK11411 245 IVKRWQQDPLWQMLTAAKKQQVASVDSNTWARMRGI---FAAERIAKDTVKI 293
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
61-225 |
3.55e-10 |
|
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238561 [Multi-domain] Cd Length: 186 Bit Score: 58.59 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 61 KKPERIITLTNSDMGIVYALGGS--VVGRQTMDASGVEPS-AALKATEVGNTHDLNLEKIASLTPDVIIASS-EQNLKDV 136
Cdd:cd01141 6 VPPKRIVVLSPTHVDLLLALDKAdkIVGVSASAYDLNTPAvKERIDIQVGPTGSLNVELIVALKPDLVILYGgFQAQTIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 137 PALEGIGAQVVLTGANS----IAD-IKKQEAILGQLLGKDAtnlQKEIDQKVAeiKQEQTGKAVRAL----LILGAPGSN 207
Cdd:cd01141 86 DKLEQLGIPVLYVNEYPsplgRAEwIKFAAAFYGVGKEDKA---DEAFAQIAG--RYRDLAKKVSNLnkptVAIGKPVKG 160
|
170 180
....*....|....*....|
gi 738133139 208 --YAALPNSLSGDILEAAGG 225
Cdd:cd01141 161 lwYMPGGNSYVAKMLRDAGG 180
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
64-324 |
3.19e-08 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 53.92 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 64 ERIITLTNSDMGIVYALGGSVVGrqtMDASGVEPSAALKATEVGNTHDLNLEKIASLTPDVIIASSEQNL-KDVPALEGI 142
Cdd:PRK03379 18 PRVITLSPANTELAFAAGITPVG---VSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAWRGGNAeRQVDQLASL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 143 GAQVVLTGANSIADIKkqeAILGQLLG-----KDATNLQKEIDQKVAEIKQEQTGKA-VRALLILgapGSN--YAALPNS 214
Cdd:PRK03379 95 GIKVMWVDATSIEQIA---NALRQLAPwspqpEKAEQAAQSLLQQYAALKAQYADKPkKRVFLQF---GTNplFTSGKHS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 215 LSGDILEAAGGVNVAKDFKgvENFPQyasLNIEKIVESDPEVIflmIHGGDEKETElafqkemKQNDAWNSTTAVKnnhI 294
Cdd:PRK03379 169 IQSQVLSLCGGENIFADSR--VPWPQ---VSREQVLARKPQAI---VITGGPDQIP-------KIKQFWGPQLKIP---V 230
|
250 260 270
....*....|....*....|....*....|
gi 738133139 295 VVLPADLFgTNPGIRITKALDYMANELNQV 324
Cdd:PRK03379 231 IPLNSDWF-ERASPRIILAAQQLCNALSQV 259
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
48-224 |
7.79e-07 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 49.97 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 48 TITDMAGrTINFAKKPERI----ITLTnsdmGIVYALGGSVVG-----------------RQ---TMDASGVEPsaaLKA 103
Cdd:PRK10957 30 TVTDSRG-SVTLESKPQRIvstsVTLT----GTLLAIDAPVIAsgattpntrvaddqgffRQwsdVAKERGVEV---LYI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738133139 104 TEVgnthdlNLEKIASLTPDVIIASS---EQNLKDVPALEGIGAQVVLT-GANSIADIKKQeaiLGQLLG--KDATNLQK 177
Cdd:PRK10957 102 GEP------DAEAVAAQMPDLIVISAtggDSALALYDQLSAIAPTLVIDyDDKSWQELATQ---LGEATGleKQAAAVIA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 738133139 178 EIDQKVAEIKQEQTGKA--VRALLILGAPGSNYAALPNSLSGDILEAAG 224
Cdd:PRK10957 173 QFDAQLAEVKAKITLPPqpVSALVYNGAGHSANLWTPESAQGQLLEQLG 221
|
|
| |
